Colour plates

A F Cuthbertson and C Thomson

Electrostatic potentials of tumour promoters

Colour Plate 1. Quantum mechanical electrostatic potential displayed on the van der Waals surface for the 40HS (a)-(c) and 40Mep (d)-(f) model compounds. The colour scale is in increments of 0.015 au bctwcen successive colours with red -0.045 au, yellow 0.000 au and dark blue 0.045 au

P L Chau and P M Dean

Molecular recognition: 3D surface structure comparison by gnomonic projection

Colour Plate 1. Molecular electrostatic potential of STX mapped onto the visible hemispherical accessible surface aligned with the matched face of the 8-atom match facing the viewer. Tessellation frequency {3,5 +},o,O

88

Colour Plate 2. Molecular electrostatic mapped onto the visible hemispherical aligned in the g-atom match corresponding in Colour Plate I

Journal

potential of TTX accessible surface to the view shown

of Molecular

Graphics

K Toma

Simple protein model building tool

Colour Plate 1. Alpha gives both the front and side view of the protein model (al-anti trypsin (see Reference 7) is shown in this example)

Colour Plate 2. In modelling session, the structure is divided into two parts (purple and orange), which can be rotated using dials. The template structure (green) can be seen in the background

Colour Plate 3. Hydrophilic amino-acids are represented by blues spheres, hydrophobic amino-acids by red ones. White spheres: Gly and Ala, green: Pro, yellow: Cys

Colour Plate 4. Cross section view of Colour Plate 3, showing clearly the tendency for hydrophobic residues to prefer the inside and hydrophilic residues the outside

Colour Plate 3. Gnomonic projection of the molecular electrostatic potential of STX using the data from Colour Plate I

Colour Plate 4. Gnomonic projection of the molecular electrostatic potential of TTX using the data from Colour Plate 2

Volume

5 Number

2 June

1987

89

L M Carson

Ribbon models of macromolecules

Colour Plate 1. The atomic temperature factors (B) for the atoms in each residue of ubiquitin are averaged. The colours white, cyan, green, orange and red map the range from cool ( = 3.8) to hot ( = 38.6)

Colour Plate 2. Flat ribbon representation of calmodulin. The calcium ions are rendered from shaded polyhedra. Each ribbon section front and back (148 residues) consists of 12 x 7 quadrilaterals. Rendering time 30 s. Photograph from Iris

Colour Plate 3. Solid ribbon representation of the PNP trimer and substrate. Note how the ‘random’ coil surrounds the active site. 24 x 7 quadrilaterals per residue (3 x 289) rendering time 2 min. Photograph from Iris

Colour Plate 4. Solid ribbon model of ubiquitin, viewing putative protein binding face. The colour-coding by residue is as follows: R,K-blue; D,E-red; N,+magenta; T,S,Yorange; M-yellow; A,V,L,I-green; H--cyan; F-pale green; P-white; G, backbone-grey; C = Odark red; NH-dark blue

90

Journal

of Molecular

Graphics